Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 31, Problem 3P
Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Both hsp60-like and hsp70 molecular chaperonesshare an affinity for exposed hydrophobic patches on pro-teins, using them as indicators of incomplete folding. Whydo you suppose hydrophobic patches serve as critical sig-nals for the folding status of a protein?
Purification of a protein of unknown structure has been achieved. The natural protein has a molecular weight of 240,000, according to size-exclusion chromatography. Using a concentration of 6 M guanidine hydrochloride in the chromatography, a single peak can be identified as the molecular weight (MW) 60,000 of a protein. B-mercaptoethanol (BME) and guanidine hydrochloride (GHC) are used in tandem to produce proteins with mass masses of 34,000 and 26,000, respectively. The structure of this protein can be inferred from these facts.
Need help, please.
Draw an oxygen binding curve of Hb at a pH of 7.4 and another curve where all 2,3 BPG has been removed
Draw an oxygen binding curve of Hb at a pH of 7.4 and another at pH.
Draw an oxygen binding curve of Hb at a pH of 7.4 and another with a mutant Hb in which the predominant form of the protein is monomeric
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- The cDNA sequence for a secreted protein shows that it contains two Asn-X-Ser/Thr motifs but nothing is known about the glycosylation of the protein. If you consider that either or both of these sites could be glycosylated and the oligosaccharides processed to either a Man5 high mannose structure or to a sialylated complex bi-antennary structure, how many possible glycoforms of the protein would there be? Explain why it is likely that such a protein would actually have very many more glycoforms.arrow_forwardApproximate molecular weight for an unknown protein from gel-filtration experiment is 130 kDa. Thirty six mg of this pure protein was treated with excess of fluorodinitrobenzene. After the reaction and complete acid hydrolysis the mixture was found to contain 356 µg of dinitrobenzene derivative of methionine (free acid) and no other amino acid-dinitrobenzene derivatives. Is this protein consisting of single polypeptide chain or multiple subunits? If it consists of multiple subunits, then how many? From these data, can you calculate the molecular weight of the protein more precisely?arrow_forwardExploring the nuanced landscape of protein dynamics, could you elaborate on noteworthy post-translational modifications (PTMs)? I'm interested in understanding specific examples of PTMs and gaining insights into their functional mechanisms. This inquiry delves into the intricate aspects of protein modulation within a biological context."arrow_forward
- The Energetic Cost of Peptide Elongation How many ATP equivalents are consumed for each amino acid added to an elongating polypeptide chain during the process of protein synthesis?arrow_forwardPolypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.arrow_forwardConsider the phenolic hydroxyl group of a particular Tyr residue in a protein. Suppose the hydroxyl group in the unfolded protein in aqueous solution, where the group is exposed to H2O, has a pKa of 10.0. If that group is found in a hydrophobic environment in the interior of the protein when the protein is folded into its native tertiary structure, would you expect the pKa of the phenolic hydroxyl to be higher or lower in the folded protein interior than in H2O? Explain your reasoning.arrow_forward
- Loop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the rolesarrow_forwardGive the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.arrow_forwardThe hydropathy plot of a particular hyaluronan synthase is plotted by Heldermon et al and is shown below. From this plot, Heldermon et al circled six putative (or predicated) membrane domains (PMDs). Circle the six regions in the plot above you believe could be transmembrane domains of the protein and indicate why you chose those regions. Please include a description of what information a hydropathy plot gives researchers.arrow_forward
- a) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?arrow_forwardSuppose you have a solution of a protein, which contains a specific Tyr residue that has an actual (measured) pKa of 8.8. The protein binds a ligand by several noncovalent interactions, one of which is a hydrogen bond in which the Tyr phenolic hydroxyl group must serve as a hydrogen bond donor. Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl group could serve as a hydrogen bond donor at pH 8.5arrow_forwardDenaturation of Proteins The following are four levels of protein structures. Identify the inter- and intramolecular forces of attractions that stabilized each level. Level of Protein Structure Forces of Attraction Present Primary Secondary Tertiary Quaternary 2.) What is denaturation? 3.) What are denaturing agents? Give three examples and describe their effects on protein. 4.) Differentiate reversible and irreversible denaturation. 5.)Why is 70% ethanol is more effective than 100% ethanol to kill bacteria?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningHuman Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...
Biology
ISBN:9781305251052
Author:Michael Cummings
Publisher:Cengage Learning
The Cell Membrane; Author: The Organic Chemistry Tutor;https://www.youtube.com/watch?v=AsffT7XIXbA;License: Standard youtube license